Human placental tissue factor: Protease susceptibility of extracellular and cytoplasmic domains

Sara M. Whittle, S. Christine Yoder, Steven D. Carson

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

We have examined the effects of seven proteases on human placental tissue factor in Triton X-100, focusing on extracellular and cytoplasmic domains recognized by monoclonal antibodies HTF1, C28 1.1, and C28 2.1. Plasmin produced peptides recognized on Western blots by C281.1 but not HTF1. None of the other proteases destroyed the extracellular epitope without also removing the cytoplasmic epitope, and both trypsin and chymotrypsin removed the cytoplasmic epitope with little effect on the extracellular domain. Proteinase K destroyed both epitopes, as did neutrophil elastase when used at a relatively high concentration. When digests were sampled over time and reconstituted with lipids for determination of tissue factor activity, only proteinase K consistently produced a loss in tissue factor activity at four hours. After 24 hr, other enzymes also decreased the recovered activity, with the order of effectiveness elastase>trypsin>chymotrypsin.

Original languageEnglish (US)
Pages (from-to)451-459
Number of pages9
JournalThrombosis Research
Volume79
Issue number5-6
DOIs
StatePublished - Sep 15 1995

Fingerprint

Thromboplastin
Epitopes
Peptide Hydrolases
Endopeptidase K
Leukocyte Elastase
Pancreatic Elastase
Fibrinolysin
Octoxynol
Chymotrypsin
Trypsin
Western Blotting
Monoclonal Antibodies
Lipids
Peptides
Enzymes

Keywords

  • protease
  • tissue factor

ASJC Scopus subject areas

  • Hematology

Cite this

Human placental tissue factor : Protease susceptibility of extracellular and cytoplasmic domains. / Whittle, Sara M.; Yoder, S. Christine; Carson, Steven D.

In: Thrombosis Research, Vol. 79, No. 5-6, 15.09.1995, p. 451-459.

Research output: Contribution to journalArticle

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